The diversity in the vanilloid (TRPV) receptor family of ion channels
Following cloning of the vanilloid receptor 1 (VR1) at least four other related proteins have been identified. Together, these form a distinct subgroup of the transient receptor potential (TRP) family of ion channels. Members of the vanilloid receptor family (TRPV) are activated by a diverse range o...
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Published in | Trends in Pharmacological Sciences Vol. 23; no. 4; pp. 183 - 191 |
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Main Authors | , , , |
Format | Book Review Journal Article |
Language | English |
Published |
England
Elsevier Ltd
01.04.2002
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Subjects | |
Online Access | Get full text |
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Summary: | Following cloning of the vanilloid receptor 1 (VR1) at least four other related proteins have been identified. Together, these form a distinct subgroup of the transient receptor potential (TRP) family of ion channels. Members of the vanilloid receptor family (TRPV) are activated by a diverse range of stimuli, including heat, protons, lipids, phorbols, phosphorylation, changes in extracellular osmolarity and/or pressure, and depletion of intracellular Ca
2+ stores. However, VR1 remains the only channel activated by vanilloids such as capsaicin. These channels are excellent molecular candidates to fulfil a range of sensory and/or cellular roles that are well characterized physiologically. Furthermore, as novel pharmacological targets, the vanilloid receptors have potential for the development of many future disease treatments.
The five vanilloid receptors identified to date are candidates for diverse sensory and cellular roles, and thus form novel pharmacological candidates. |
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Bibliography: | ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 ObjectType-Review-3 content type line 23 ObjectType-Feature-3 ObjectType-Review-1 |
ISSN: | 0165-6147 1873-3735 |
DOI: | 10.1016/S0165-6147(02)01999-5 |